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P22534 (GUNA_CALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endoglucanase A
EC=3.2.1.4
Alternative name(s):
Cellulase A
Endo-1,4-beta-glucanase A
Gene names
Name:celA
OrganismCaldocellum saccharolyticum (Caldicellulosiruptor saccharolyticus)
Taxonomic identifier44001 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length1742 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

The N-terminal domain of CelA encodes for an endoglucanase activity on carboxymethylcellulose. The C-terminal domain probably acts synergistically to hydrolyze crystalline cellulose.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Post-translational modification

The linker region (also termed "hinge") may be a potential site for proteolysis.

Sequence similarities

In the N-terminal section; belongs to the glycosyl hydrolase 9 (cellulase E) family.

In the C-terminal section; belongs to the glycosyl hydrolase 48 (cellulase L) family.

Contains 3 CBM3 (carbohydrate binding type-3) domains.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 17421719Endoglucanase A
PRO_0000007944

Regions

Domain477 – 637161CBM3 1
Domain703 – 856154CBM3 2
Domain906 – 1059154CBM3 3
Region24 – 476453Catalytic 1
Region638 – 70265Linker ("hinge") (Pro-Thr box)
Region857 – 90549Linker ("hinge") (Pro-Thr box)
Region1060 – 111253Linker ("hinge") (Pro-Thr box)
Region1113 – 1742630Catalytic 2

Sites

Active site3961 By similarity
Active site4341 By similarity
Active site4431 By similarity

Experimental info

Sequence conflict15451T → A in AAA72860. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22534 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 3F0699A2123EED07

FASTA1,742193,697
        10         20         30         40         50         60 
MVVTFLFILG VVYGVKPWQE ARAGSFNYGE ALQKAIMFYE FQMSGKLPNW VRNNWRGDSA 

        70         80         90        100        110        120 
LKDGQDNGLD LTGGWFDAGD HVKFNLPMSY TGTMLSWAAY EYKDAFVKSG QLEHILNQIE 

       130        140        150        160        170        180 
WVNDYFVKCH PSKYVYYYQV GDGGKDHAWW GPAEVMQMER PSFKVTQSSP GSAVVAETAA 

       190        200        210        220        230        240 
SLAAASIVLK DRNPTKAATY LQHAKDLYEF AEVTKSDSGY TAANGYYNSW SGFYDELSWA 

       250        260        270        280        290        300 
AVWLYLATND STYLTKAESY VQNWPKISGS NIIDYKWAHC WDDVHNGAAL LLAKITDKDT 

       310        320        330        340        350        360 
YKQIIESHLD YWTTGYNGER IKYTPKGLAW LDQWGSLRYA TTTAFLAFVY SDWSGCPTGK 

       370        380        390        400        410        420 
KETYRKFGES QIDYALGSTG RSFVVGFGTN PPKRPHHRTA HSSWADSQSI PSYHRHTLYG 

       430        440        450        460        470        480 
ALVGGPGSDD SYTDDISNYV NNEVACDYNA GFVGALAKMY LLYGGNPIPD FKAIETPTND 

       490        500        510        520        530        540 
EFFVEAGINA SGTNFIEIKA IVNNQSGWPA RATNKLKFRY FVDLSELIKA GYSPNQLTLS 

       550        560        570        580        590        600 
TNYNQGAKVS GPYVWDSSRN IYYILVDFTG TLIYPGGQDK YKKEVQFRIA APQNVQWDNS 

       610        620        630        640        650        660 
NDYSFQDIKG VSSGSVVKTK YIPLYDEDIK VWGEEPGTSG VSPTPTASVT PTPTPTPTAT 

       670        680        690        700        710        720 
PTPTPTPTVT PTPTVTATPT PTPTPTSTPT VTPTPTPVST PATSGQIKVL YANKETNSTT 

       730        740        750        760        770        780 
NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV DGERAQSAIS DWAQIGASNV TFKFVKLSSS 

       790        800        810        820        830        840 
VSGADYYLEI GFKSGAGQLQ PGKDTGEIQI RFNKDDWSNY NQGNDWSWIQ SMTSYGENEK 

       850        860        870        880        890        900 
VTAYIDGVLV WGQEPSGTTP APTSTPTVTV TPTPTPTPTV TPTPTVTATP TPTPTPTSTP 

       910        920        930        940        950        960 
VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI DLSRVTIRYW YTVDGERAQS 

       970        980        990       1000       1010       1020 
AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG QLQPGKDTGE IQIRFNKDDW 

      1030       1040       1050       1060       1070       1080 
SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG VLVWGQEPSG ATPAPTVTPT PTVTPTPTPA 

      1090       1100       1110       1120       1130       1140 
PTPTATPTPT PTPTVTPTPT VAPTPTPSST PSGLGKYGQR FMWLWNKIHD PASGYFNQDG 

      1150       1160       1170       1180       1190       1200 
IPYHSVETLI CEAPDYGHLT TSEAFSYYVW LEAVYGKLTG DWSKFKTAWD TLEKYMIPSA 

      1210       1220       1230       1240       1250       1260 
EDQPMRSYDP NKPATYAGEW ETPDKYPSPL EFNVPVGKDP LHNELVSTYG STLMYGMHWL 

      1270       1280       1290       1300       1310       1320 
MDVDNWYGYG KRGDGVSRAS FINTFQRGPE ESVWETVPHP SWEEFKWGGP NGFLDLFIKD 

      1330       1340       1350       1360       1370       1380 
QNYSKQWRYT NAPDADARAI QATYWAKVWA KEQGKFNEIS SYVGKAAKMG DYLRYAMFDK 

      1390       1400       1410       1420       1430       1440 
YFKPLGCQDK NAAGGTGYDS AHYLLSWYYA WGGALDGAWS WKIGCSHAHF GYQNPMAAWA 

      1450       1460       1470       1480       1490       1500 
LANDSDMKPK SPNGASDWAK SLKRQIEFYR WLQSAEGAIA GGATNSWNGR YEKYPAGTAT 

      1510       1520       1530       1540       1550       1560 
FYGMAYEPNP VYRDPGSNTW FGFQAWSMQR VAEYYYVTGD KDAGTLLEKW VSWIKSVVKL 

      1570       1580       1590       1600       1610       1620 
NSDGTFAIPS TLDWSGQPDT WNGTYTGNPN LHVKVVDYGT DLGITASLAN ALLYYSAGTK 

      1630       1640       1650       1660       1670       1680 
KYGVFDEEAK NLAKELLDRM WKLYRDEKGL SAPEKRADYK RFFEQEVYIP AGWTGKMPNG 

      1690       1700       1710       1720       1730       1740 
DVIKSGVKFI DIRSKYKQDP DWPKLEAAYK SGQVPEFRYH RFWAQCDIAI VNATYEILFG 


NQ

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References

[1]"celA, another gene coding for a multidomain cellulase from the extreme thermophile Caldocellum saccharolyticum."
Te'O V.S. Jr., Saul D.J., Bergquist P.L.
Appl. Microbiol. Biotechnol. 43:291-296(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum'."
Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L.
Appl. Environ. Microbiol. 57:694-700(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1516-1742.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L32742 Genomic DNA. Translation: AAA91086.1.
M36063 Genomic DNA. Translation: AAA72860.1.
L01257 Unassigned DNA. No translation available.
PIRT17120.

3D structure databases

ProteinModelPortalP22534.
SMRP22534. Positions 26-636, 1117-1739.
ModBaseSearch...

Protein family/group databases

CAZyCBM3. Carbohydrate-Binding Module Family 3.
GH48. Glycoside Hydrolase Family 48.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 5 hits.
2.60.40.710. 3 hits.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR000556. Glyco_hydro_48F.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
[Graphical view]
PfamPF00942. CBM_3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
PRINTSPR00844. GLHYDRLASE48.
SMARTSM01067. CBM_3. 3 hits.
[Graphical view]
SUPFAMSSF49384. Cellul_bind. 3 hits.
SSF48208. Glyco_trans_6hp. 2 hits.
PROSITEPS51172. CBM3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUNA_CALSA
AccessionPrimary (citable) accession number: P22534
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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